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Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8

Authors :
Nicholas Muzyczka
Barry J. Byrne
Eric Padron
Robert McKenna
Hyun Joo Nam
George Aslanidi
Michael Douglas Lane
Brittney Gurda-Whitaker
Mavis Agbandje-McKenna
Sergei Zolotukhin
Eric Kohlbrenner
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 6)
Publication Year :
2005

Abstract

Adeno-associated viruses (AAVs) are actively being developed for clinical gene-therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue-transduction interactions. AAV8 is approximately 80% identical to the more widely studied AAV2, but its liver-transduction efficiency is significantly greater than that of AAV2 and other serotypes. The production, purification, crystallization and preliminary X-ray crystallographic analysis of AAV8 viral capsids are reported. The crystals diffract X-rays to 3.0 A resolution using synchrotron radiation and belong to the hexagonal space group P6(3)22, with unit-cell parameters a = 257.5, c = 443.5 A. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit.

Details

ISSN :
17443091
Volume :
61
Issue :
Pt 6
Database :
OpenAIRE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Accession number :
edsair.doi.dedup.....845d6d710f997ea146b07f91e92c3917